| IED ID | IndEnz0002008236 |
| Enzyme Type ID | protease008236 |
| Protein Name |
Calmodulin-dependent glutamylase SidJ EC 6.-.-.- |
| Gene Name | sidJ lpg2155 |
| Organism | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Legionellales Legionellaceae Legionella Legionella pneumophila Legionella pneumophila subsp. pneumophila Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Enzyme Sequence | MFGFIKKVLDFFGVDQSEDNPSETAVETTDVSTKIKTTDTTQEESSVKTKTVVPTQPGGSVKPETIAPDQQKKHQIKTETTTSTTKQKGPKVTLMDGHVKQYYFARRGETSTHDTSLPPPVKVLSGRSIPLKEIPFEATRNELVQIYLTSIDKLIKSNKLNSIPSQQIASHYLFLRSLANSETDGIKKNQILSLAKPLGTYLASKEPHVWKMINELIEKSEYPIIHYLKNNRAHSNFMLALIHEYHKEPLTKNQSAFVQKFRDSSVFLFPNPIYTAWLAHSYDEDSSFNPMFRERLSTNFYHSTLTDNLLLRTEPKEVTLSSEHHYKKEKGPIDSSFRYQMSSDRLLRIQGRTLLFSTPQNDVVAVKVQKKGEPKSTLEEEFEMADYLLKHQRRLDVHSKLPQPLGQYSVKKSEILEISRGSLDFERFKTLIDDSKDLEVYVYKAPQSYFTYLHDKNQDLEDLTASVKTNVHDLFVLLREGIVFPQLADIFHTHFGEDEREDKGRYQALVQLLNVLQFQLGRIDKWQKAVEYVNLRSSGLADLGDSLPITSLFTSSDFTKHYFSELLTGGYHPTFFDKSSGTANSLFTGKRRLFGNYLYLNTIAEYLLVIQLTLGSYGDKVTRDMMDKPKKEAVWRELANVMFTSCAEAIHIMTGIPQSRALTLLKQRANIEKHFRQTQFWMTPDYSKLDEDTLQMEQYSIYSGEPEYEFTDKLVSGVGLSVDGVHQDLGGYNRESPLRELEKLLYATVTLIEGTMQLDKEFFKQLEQVEKILSGEIKTDANSCFEAVAQLLDLARPGCHFQKRLVLSYYEEAKLKYPSAPTDAYDSRFQVVARTNAAITIQRFWREARKNLSEKSDIDSEKPESERTTDKRL |
| Enzyme Length | 873 |
| Uniprot Accession Number | Q5ZTK6 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Glytamylation catalyzed by SidJ requires host calmodulin and can be regulated by intracellular changes in Ca2+ concentrations. Requires also ATP. {ECO:0000269|PubMed:31123136, ECO:0000269|PubMed:31330531}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + L-glutamyl-[protein] = ADP + gamma-L-glutamyl-L-glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:60144, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15517, ChEBI:CHEBI:15378, ChEBI:CHEBI:29973, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143622, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31123136, ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}; CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:31123136, ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}; |
| DNA Binding | |
| EC Number | 6.-.-.- |
| Enzyme Function | FUNCTION: Glutamylase that mediates the covalent attachment of glutamate moieties to SdeA on one of the catalytic residues that is required for its mono-ADP-ribosyltransferase activity (PubMed:31330532, PubMed:31330531). In turn, inhibits SdeA ubiquitinating activity. Glutamylates also related SdeB, SdeC and SidE (PubMed:31330531, PubMed:31123136). Glutamylase activity only occurs in the host since it requires host calmodulin (PubMed:28497808, PubMed:31330532, PubMed:31330531, PubMed:31123136). May also reverse the SdeA-mediated substrate ubiquitination by cleaving the phosphodiester bond that links phosphoribosylated ubiquitin to protein substrates via its deubiquitinase activity (PubMed:28497808). {ECO:0000269|PubMed:28497808, ECO:0000269|PubMed:31123136, ECO:0000269|PubMed:31330531, ECO:0000269|PubMed:31330532}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (23); Chain (1); Compositional bias (1); Helix (36); Metal binding (2); Mutagenesis (2); Region (2); Turn (9) |
| Keywords | 3D-structure;Hydrolase;Ligase;Magnesium;Metal-binding;Multifunctional enzyme;NAD;Nucleotide-binding;Protease;Reference proteome;Thiol protease;Transferase;Virulence |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (5); X-ray crystallography (5) |
| Cross Reference PDB | 6K4K; 6K4L; 6K4R; 6OQQ; 6PLM; 6S5T; 7MIR; 7MIS; 7PPO; 7PQE; |
| Mapped Pubmed ID | 31682223; 34407442; 34702826; |
| Motif | |
| Gene Encoded By | |
| Mass | 100,201 |
| Kinetics | |
| Metal Binding | METAL 542; /note="Magnesium"; /evidence="ECO:0000269|PubMed:31123136, ECO:0007744|PDB:6OQQ"; METAL 545; /note="Magnesium"; /evidence="ECO:0000269|PubMed:31123136, ECO:0007744|PDB:6OQQ" |
| Rhea ID | RHEA:60144; RHEA:60148 |
| Cross Reference Brenda |